A new strategy for caging proteins regulated by kinases

Mousumi Ghosh, Ilia Ichetovkin, Xiaoyan Song, John S. Condeelis, David S. Lawrence

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

A strategy has been developed for caging proteins that are endogenously regulated by phosphorylation. A key phosphorylatable serine in cofilin, an F-actin cleaving protein, was replaced with a nonphosphorylatable cysteine. The latter conversion ensures that the protein is no longer regulated by endogenous protein kinases. The cysteine residue was subsequently covalently modified with a negatively charged caging moiety, which electrostatically mimics the natural serine phosphate present in the inactive wild-type protein. Photoremoval of the cage generates an active protein, which cannot be switched off by endogenous protein kinases. Caged cofilin, and its irradiated counterpart, display the anticipated F-actin depolymerization and severing activities.

Original languageEnglish (US)
Pages (from-to)2440-2441
Number of pages2
JournalJournal of the American Chemical Society
Volume124
Issue number11
DOIs
StatePublished - Mar 20 2002

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Protein Kinases
Phosphotransferases
Proteins
Actin Depolymerizing Factors
Cysteine
Actins
Phosphoserine
Depolymerization
Phosphorylation
Serine
Phosphates

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

A new strategy for caging proteins regulated by kinases. / Ghosh, Mousumi; Ichetovkin, Ilia; Song, Xiaoyan; Condeelis, John S.; Lawrence, David S.

In: Journal of the American Chemical Society, Vol. 124, No. 11, 20.03.2002, p. 2440-2441.

Research output: Contribution to journalArticle

Ghosh, Mousumi ; Ichetovkin, Ilia ; Song, Xiaoyan ; Condeelis, John S. ; Lawrence, David S. / A new strategy for caging proteins regulated by kinases. In: Journal of the American Chemical Society. 2002 ; Vol. 124, No. 11. pp. 2440-2441.
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